| pubmed-article:8914516 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8914516 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:8914516 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:8914516 | lifeskim:mentions | umls-concept:C1314792 | lld:lifeskim |
| pubmed-article:8914516 | lifeskim:mentions | umls-concept:C1457869 | lld:lifeskim |
| pubmed-article:8914516 | lifeskim:mentions | umls-concept:C1836606 | lld:lifeskim |
| pubmed-article:8914516 | lifeskim:mentions | umls-concept:C1749524 | lld:lifeskim |
| pubmed-article:8914516 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8914516 | pubmed:dateCreated | 1996-12-16 | lld:pubmed |
| pubmed-article:8914516 | pubmed:abstractText | In a search for proteins associated with Rna15p in processing the 3' ends of messenger RNAs, we have looked for suppressors that correct, even partially, the thermosensitive growth defect of the rna15-2 mutant. Mutations in a single locus that we named SSM5, were able to suppress both the thermosensitivity of cell growth and the mRNA 3' processing defect associated with the rna15-2 mutation, but only slightly alleviated the thermosensitive growth defect of an rna14-1 mutant. The ssm5-1 mutant is sensitive to hydroxyurea at 37 degrees C, a drug that inhibits DNA synthesis. By screening for complementation of the hydroxyurea-sensitive phenotype we cloned the corresponding wild-type gene and found that it corresponds to the essential gene STS1 (also named DBF8). Sts1p has an apparent molecular weight of 30 kDa and was confirmed to be a cytosolic protein by immunofluorescence analysis. Western blot analysis indicates that the thermosensitive mutant strains rna15-2, rna14-1 and pap1-1 present a very low level of the Rna15p at 37 degrees C. The ssm5-1 mutation restores the level of Rna15p in the rna15-2 ssm5-1 double mutant. Use of the two-hybrid system suggests that Sts1p does not interact directly with Rna15p, but may be active as a homodimer. The present data suggest that Sts1p may play a role in the transport of Rna15p from the cytoplasm to the nucleus. | lld:pubmed |
| pubmed-article:8914516 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8914516 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8914516 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8914516 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8914516 | pubmed:issn | 0026-8925 | lld:pubmed |
| pubmed-article:8914516 | pubmed:author | pubmed-author:LacrouteFF | lld:pubmed |
| pubmed-article:8914516 | pubmed:author | pubmed-author:AmraniNN | lld:pubmed |
| pubmed-article:8914516 | pubmed:author | pubmed-author:DufourM EME | lld:pubmed |
| pubmed-article:8914516 | pubmed:author | pubmed-author:BonneaudNN | lld:pubmed |
| pubmed-article:8914516 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8914516 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:8914516 | pubmed:volume | 252 | lld:pubmed |
| pubmed-article:8914516 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8914516 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8914516 | pubmed:pagination | 552-62 | lld:pubmed |
| pubmed-article:8914516 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8914516 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8914516 | pubmed:articleTitle | Mutations in STS1 suppress the defect in 3' mRNA processing caused by the rna15-2 mutation in Saccharomyces cerevisiae. | lld:pubmed |
| pubmed-article:8914516 | pubmed:affiliation | Centre de Génétique Moléculaire du C.N.R.S., Laboratoire propre associé à I'Université Pierre et Marie Curie, Gif sur Yvette, France. | lld:pubmed |
| pubmed-article:8914516 | pubmed:publicationType | Journal Article | lld:pubmed |
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